메뉴 건너뛰기




Volumn 19, Issue 2, 2005, Pages 171-181

Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2

Author keywords

[No Author keywords available]

Indexed keywords

HEME; IRON REGULATORY PROTEIN 2; UBIQUITIN PROTEIN LIGASE;

EID: 22544452148     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.05.027     Document Type: Article
Times cited : (138)

References (41)
  • 2
    • 0040992183 scopus 로고
    • Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5
    • S. Beck von Bodman, M.A. Schuler, D.R. Jollie, and S.G. Sligar Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5 Proc. Natl. Acad. Sci. USA 83 1986 9443 9447
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9443-9447
    • Beck Von Bodman, S.1    Schuler, M.A.2    Jollie, D.R.3    Sligar, S.G.4
  • 3
    • 0348111398 scopus 로고    scopus 로고
    • The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2
    • E. Bourdon, D.K. Kang, M.C. Ghosh, S.K. Drake, J. Wey, R.L. Levine, and T.A. Rouault The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2 Blood Cells Mol. Dis. 31 2003 247 255
    • (2003) Blood Cells Mol. Dis. , vol.31 , pp. 247-255
    • Bourdon, E.1    Kang, D.K.2    Ghosh, M.C.3    Drake, S.K.4    Wey, J.5    Levine, R.L.6    Rouault, T.A.7
  • 4
    • 0025965045 scopus 로고
    • Amino acid microsequencing of internal tryptic peptides of heme-regulated eukaryotic initiation factor 2 α subunit kinase: Homology to protein kinases
    • J.J. Chen, J.K. Pal, R. Petryshyn, I. Kuo, J.M. Yang, M.S. Throop, L. Gehrke, and I.M. London Amino acid microsequencing of internal tryptic peptides of heme-regulated eukaryotic initiation factor 2 α subunit kinase: homology to protein kinases Proc. Natl. Acad. Sci. USA 88 1991 315 319
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 315-319
    • Chen, J.J.1    Pal, J.K.2    Petryshyn, R.3    Kuo, I.4    Yang, J.M.5    Throop, M.S.6    Gehrke, L.7    London, I.M.8
  • 5
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • P. Chen, P. Johnson, T. Sommer, S. Jentsch, and M. Hochstrasser Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor Cell 74 1993 357 369
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 6
    • 0014217153 scopus 로고
    • The interaction of nucleotides with the active site of staphylococcal nuclease. Spectrophotometric studies
    • P. Cuatrecasas, S. Fuchs, and C.B. Anfinsen The interaction of nucleotides with the active site of staphylococcal nuclease. Spectrophotometric studies J. Biol. Chem. 242 1967 4759 4767
    • (1967) J. Biol. Chem. , vol.242 , pp. 4759-4767
    • Cuatrecasas, P.1    Fuchs, S.2    Anfinsen, C.B.3
  • 7
    • 0021070823 scopus 로고
    • The diverse spectroscopic properties of ferrous cytochrome P-450-CAM ligand complexes
    • J.H. Dawson, L.A. Andersson, and M. Sono The diverse spectroscopic properties of ferrous cytochrome P-450-CAM ligand complexes J. Biol. Chem. 258 1983 13637 13645
    • (1983) J. Biol. Chem. , vol.258 , pp. 13637-13645
    • Dawson, J.H.1    Andersson, L.A.2    Sono, M.3
  • 8
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 9
    • 0032524657 scopus 로고    scopus 로고
    • Involvement of heme in the degradation of iron-regulatory protein 2
    • L.S. Goessling, D.P. Mascotti, and R.E. Thach Involvement of heme in the degradation of iron-regulatory protein 2 J. Biol. Chem. 273 1998 12555 12557
    • (1998) J. Biol. Chem. , vol.273 , pp. 12555-12557
    • Goessling, L.S.1    Mascotti, D.P.2    Thach, R.E.3
  • 10
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • B. Guo, J.D. Phillips, Y. Yu, and E.A. Leibold Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome J. Biol. Chem. 270 1995 21645 21651
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 11
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • E.S. Hanson, M.L. Rawlins, and E.A. Leibold Oxygen and iron regulation of iron regulatory protein 2 J. Biol. Chem. 278 2003 40337 40342
    • (2003) J. Biol. Chem. , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3
  • 12
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • M.W. Hentze, M.U. Muckenthaler, and N.C. Andrews Balancing acts: molecular control of mammalian iron metabolism Cell 117 2004 285 297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 13
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • K. Iwai, R.D. Klausner, and T.A. Rouault Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2 EMBO J. 14 1995 5350 5357
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 15
    • 8544244946 scopus 로고    scopus 로고
    • Identification of a heme-sensing domain in iron regulatory protein 2
    • J. Jeong, T.A. Rouault, and R.L. Levine Identification of a heme-sensing domain in iron regulatory protein 2 J. Biol. Chem. 279 2004 45450 45454
    • (2004) J. Biol. Chem. , vol.279 , pp. 45450-45454
    • Jeong, J.1    Rouault, T.A.2    Levine, R.L.3
  • 16
    • 0038013736 scopus 로고    scopus 로고
    • Iron regulatory protein 2 as iron sensor. Iron-dependent oxidative modification of cysteine
    • D.K. Kang, J. Jeong, S.K. Drake, N.B. Wehr, T.A. Rouault, and R.L. Levine Iron regulatory protein 2 as iron sensor. Iron-dependent oxidative modification of cysteine J. Biol. Chem. 278 2003 14857 14864
    • (2003) J. Biol. Chem. , vol.278 , pp. 14857-14864
    • Kang, D.K.1    Jeong, J.2    Drake, S.K.3    Wehr, N.B.4    Rouault, T.A.5    Levine, R.L.6
  • 17
    • 0347624596 scopus 로고    scopus 로고
    • S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway
    • S. Kim, S.S. Wing, and P. Ponka S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway Mol. Cell. Biol. 24 2004 330 337
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 330-337
    • Kim, S.1    Wing, S.S.2    Ponka, P.3
  • 18
    • 0027405813 scopus 로고
    • Regulation by heme of mitochondrial protein transport through a conserved amino acid motif
    • J.T. Lathrop, and M.P. Timko Regulation by heme of mitochondrial protein transport through a conserved amino acid motif Science 259 1993 522 525
    • (1993) Science , vol.259 , pp. 522-525
    • Lathrop, J.T.1    Timko, M.P.2
  • 21
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • E.G. Meyron-Holtz, M.C. Ghosh, and T.A. Rouault Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo Science 306 2004 2087 2090
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 22
  • 24
    • 0024979286 scopus 로고
    • Functional dissection and sequence of yeast HAP1 activator
    • K. Pfeifer, K.S. Kim, S. Kogan, and L. Guarente Functional dissection and sequence of yeast HAP1 activator Cell 56 1989 291 301
    • (1989) Cell , vol.56 , pp. 291-301
    • Pfeifer, K.1    Kim, K.S.2    Kogan, S.3    Guarente, L.4
  • 25
    • 0036161801 scopus 로고    scopus 로고
    • Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis
    • Z. Qi, and M.R. O'Brian Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis Mol. Cell 9 2002 155 162
    • (2002) Mol. Cell , vol.9 , pp. 155-162
    • Qi, Z.1    O'Brian, M.R.2
  • 26
    • 0033539642 scopus 로고    scopus 로고
    • Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein
    • Z. Qi, I. Hamza, and M.R. O'Brian Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein Proc. Natl. Acad. Sci. USA 96 1999 13056 13061
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13056-13061
    • Qi, Z.1    Hamza, I.2    O'Brian, M.R.3
  • 28
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation
    • F. Samaniego, J. Chin, K. Iwai, T.A. Rouault, and R.D. Klausner Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation J. Biol. Chem. 269 1994 30904 30910
    • (1994) J. Biol. Chem. , vol.269 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Rouault, T.A.4    Klausner, R.D.5
  • 29
    • 0037352408 scopus 로고    scopus 로고
    • Haemin uptake and use as an iron source by Candida albicans: Role of CaHMX1-encoded haem oxygenase
    • R. Santos, N. Buisson, S. Knight, A. Dancis, J.M. Camadro, and E. Lesuisse Haemin uptake and use as an iron source by Candida albicans: role of CaHMX1-encoded haem oxygenase Microbiol. 149 2003 579 588
    • (2003) Microbiol. , vol.149 , pp. 579-588
    • Santos, R.1    Buisson, N.2    Knight, S.3    Dancis, A.4    Camadro, J.M.5    Lesuisse, E.6
  • 30
    • 4544220638 scopus 로고    scopus 로고
    • Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide?
    • S. Sassa Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide? Antioxid. Redox Signal. 6 2004 819 824
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 819-824
    • Sassa, S.1
  • 31
    • 0017367091 scopus 로고
    • Induction of aminolevulinate synthase and porphyrins in cultured liver cells maintained in chemically defined medium. Permissive effects of hormones on induction process
    • S. Sassa, and A. Kappas Induction of aminolevulinate synthase and porphyrins in cultured liver cells maintained in chemically defined medium. Permissive effects of hormones on induction process J. Biol. Chem. 252 1977 2428 2436
    • (1977) J. Biol. Chem. , vol.252 , pp. 2428-2436
    • Sassa, S.1    Kappas, A.2
  • 33
    • 0025203672 scopus 로고
    • Molecular cloning, sequencing, and expression of mouse ferrochelatase
    • S. Taketani, Y. Nakahashi, T. Osumi, and R. Tokunaga Molecular cloning, sequencing, and expression of mouse ferrochelatase J. Biol. Chem. 265 1990 19377 19380
    • (1990) J. Biol. Chem. , vol.265 , pp. 19377-19380
    • Taketani, S.1    Nakahashi, Y.2    Osumi, T.3    Tokunaga, R.4
  • 34
    • 0032566713 scopus 로고    scopus 로고
    • Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity
    • S. Taoka, S. Ohja, X. Shan, W.D. Kruger, and R. Banerjee Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity J. Biol. Chem. 273 1998 25179 25184
    • (1998) J. Biol. Chem. , vol.273 , pp. 25179-25184
    • Taoka, S.1    Ohja, S.2    Shan, X.3    Kruger, W.D.4    Banerjee, R.5
  • 35
    • 0347991814 scopus 로고    scopus 로고
    • Histidine and lysine as targets of oxidative modification
    • K. Uchida Histidine and lysine as targets of oxidative modification Amino Acids 25 2003 249 257
    • (2003) Amino Acids , vol.25 , pp. 249-257
    • Uchida, K.1
  • 36
    • 1642458415 scopus 로고    scopus 로고
    • Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity
    • J. Wang, G. Chen, M. Muckenthaler, B. Galy, M.W. Hentze, and K. Pantopoulos Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity Mol. Cell. Biol. 24 2004 954 965
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 954-965
    • Wang, J.1    Chen, G.2    Muckenthaler, M.3    Galy, B.4    Hentze, M.W.5    Pantopoulos, K.6
  • 37
    • 0035808315 scopus 로고    scopus 로고
    • Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase
    • C.C. Wei, Z.Q. Wang, Q. Wang, A.L. Meade, C. Hemann, R. Hille, and D.J. Stuehr Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase J. Biol. Chem. 276 2001 315 319
    • (2001) J. Biol. Chem. , vol.276 , pp. 315-319
    • Wei, C.C.1    Wang, Z.Q.2    Wang, Q.3    Meade, A.L.4    Hemann, C.5    Hille, R.6    Stuehr, D.J.7
  • 38
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a β-TrCP1-Skp1-β-catenin complex: Destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase
    • G. Wu, G. Xu, B.A. Schulman, P.D. Jeffrey, J.W. Harper, and N.P. Pavletich Structure of a β-TrCP1-Skp1-β-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase Mol. Cell 11 2003 1445 1456
    • (2003) Mol. Cell , vol.11 , pp. 1445-1456
    • Wu, G.1    Xu, G.2    Schulman, B.A.3    Jeffrey, P.D.4    Harper, J.W.5    Pavletich, N.P.6
  • 41
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • L. Zhang, and L. Guarente Heme binds to a short sequence that serves a regulatory function in diverse proteins EMBO J. 14 1995 313 320
    • (1995) EMBO J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.